期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 58, 期 6, 页码 3840-3846出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf904300q
关键词
Sepia officinalis; muscle protein hydrolysates; ACE inhibitory peptide; purification and identification
资金
- Ministry of Higher Education, Scientific Research and Technology, Tunisia
The angiotensin I-converting enzyme (ACE) inhibitory activities of protein hydrolysates prepared from cuttlefish (Sepia officinalis) proteins by treatment with various bacterial proteases were investigated. The hydrolysate generated by the crude enzyme from Bacillus mojavensis A21 displayed the highest ACE inhibitory activity, and the higher inhibition activity (87.11 +/- 0.92% at 2 mg/mL) was obtained with hydrolysis degree of 16%. This hydrolysate was fractionated by size exclusion chromatography on a Sephadex G-25 into eight major fractions (P-1-P-8). Fraction P-6, which exhibited the highest ACE inhibitory activity, was then fractionated by reversed-phase high performance liquid chromatography (RIP-HPLC). Eleven ACE inhibitory peptides were isolated, and their molecular masses and amino acids sequences were determined using ESI-MS and ESI-MS/MS, respectively. The structures of the most potent peptides were identified as Ala-His-Ser-Tyr, Gly-Asp-Ala-Pro, Ala-Gly-Ser-Pro and Asp-Phe-Gly. The first peptide displayed the highest ACE inhibitory activity with an IC50 of 11.6 mu M. The results of this study suggest that cuttlefish protein hydrolysates are a good source of ACE inhibitory peptides.
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